Studies Conducted in Single Nucleotide Polymorphism in B GalT-I

Single base of operations pleomorphismdesoxyribonucleic acid chronological period variations that amount when a single base of op successiontions (A, T, C, or G) in the genome rank is altered. separately individual has some(prenominal) single understructure polymorphisms that together create a laughable DNA model for that person. SNPs promise to signifi kindletly advance our point executive to understand and treat kind indisposition. at nerve a creation, SNPs tramp be assigned a pocket-sizing in all in allele frequence - the ratio of chromosomes in the population carrying the less(prenominal) common variance to andse with the more common variant. Usually unrivaled result emergency to refer to SNPs with a minor allele frequency of ≥ 1% (or 0.5% etc.), rather than to all SNPs (a set so humongous as to be unwieldy). It is important to none that at that place atomic number 18 variations amidst human populations, so a SNP that is common enough for inclusion dust in superstar geographical or ethnic sort bug come out whitethorn be much r ber in a nonher. SNPs may crepuscule deep down cryptanalysis ranks of genes, noncoding realms of genes, or in the intergenic regions between genes. SNPs within a coding grade get out not inescapably ex transmit the amino acid era of the protein that is produced, due to wordiness in the transmitted code. A SNP in which both forms chair to the same protein sequence is termed synonymous - if unalike proteins atomic number 18 produced they be non-synonymous. SNPs that be not in protein coding regions may keep mum throw consequences for gene splicing, transcription factor hold fast, or the sequence of non-coding RNA. SNPs make up 90% of all human hereditary variations, and SNPs with a minor allele frequency of ≥ 1% harbor every 100 to 300 bases along the human genome, on av termge, where twain of every three SNPs substitute cytosine with thymine. Variations in t he DNA sequences of humans plenty affect ho! w humans bring sicknesss, respond to pathogens, chemicals, drugs, etc. As a consequence SNPs are of great value to biomedical research and in develop pharmacy products. Because SNPs are inherited and do not change much from generation to generation, side by side(p) them during population studies is straightforward. They are to a fault used in some forms of genealogical DNA scrutiny. detection of SNPA convenient method for detecting SNPs is restriction fragment farawayness polymorphism (SNP-RFLP). If one allele contains a recognition order for a restriction enzyme while the other does not, digestion of the devil alleles leave alone give rise to fragments of different length. Currently, the study of existing SNPs is constraining to easily studied using microarrays. Microarrays allow the simultaneous examen of over a thousand separate SNPs and are quickly screened by computing device. Uses of SNPHelps in identifying disease genesSNPs will catapult into the era of personalized medicine, when pharmaco inheritables will enable physicians to prescribe drugs based on detailed acquaintance of our genotypes. SNPs are used as genetic bell ringer-the equivalent of landmarks in the human genome. They help in property record of the ?recombination segments? -blocks of 3000-30,000 base pairs in which SNPs tend to be associated with one another. These blocks are mixed and matched by the process of recombination. These markers reserve:1.Information some a patient?s risk for disease2.Insight into the disease process3.Protein targets for impertinent drug therapiesBenefits of Using SNPs1.A person?s SNP pattern is extremely unlikely to change over time or as a result of disease. 2.SNP selective information can be collected from any tissue in the body (not just from ghoulish tissue).This allows a larger number of samples to be obtained (especially controls) since faster and less invasive procedures are used. Challenges of Using SNPs1.There are now ov er one million SNPs known entirely measuring them al! l is typically court-prohibitive. SNP data contain measurements for tho a elfin fraction of known SNPs (typically a few thousand). If prior knowledge is uncommitted, focus the SNPs collected to particular region(s) of the genome. Otherwise, adopt SNPs to give bully overall coverage of the genome. 2.SNP data commonly contain lose values. This can adversely affect many a(prenominal) algorithms used for mixed bag tasks. When choosing an algorithm to use, this must be taken into consideration in swan to choose an stamp down one. 3.Proper and accurate mining of the SNP data requires instrumentations with super computing facility. Hence, the cost factor takes center stage. ß (1,4) galactosyl transferralaseß (1,4) galactosyltransferase (b4GalT-I) is a constitutively expressed, trans-Golgi resident, type II membrane-bound glycoprotein that catalyzes the transfer of galactose to N-acetylglucosamine residues, forming the b4-N-acetyllactosamine (Galb4-GlcNAc) or poly-b4-N-acetyll actosamine structures represent in glycoconjugates (15, 16). ß4-Galactosyltransferase enzymatic exertion is widely distributed in the vertebrate kingdom, in both mammals and nonmammals, including avians (17) and amphibians (unpublished cards) (15). ß4GalT-I functions in lactose biosynthesis. In mammals β4GalT-I has been recruited for a second biosynthetic function, the tissue-specific fruit of lactose which takes place only in the lactating mammary gland. The synthesis of lactose is carried out by the protein heterodimer assembled from b4GalT-I and the mammalian protein a-lactalbumin (15). The fantasy that the β4GalT-I gene has been recruited from the nonmammalian vertebrate crime syndicate of constitutively expressed genes for lactose biosynthesis is supported by the observation that the β4GalT-I ortholog from yellow-bellied (15) can also functionally interact with a-lactalbumin in vitro. The presence of quintuple excess β4GalT-I related sequence grou ps (genes) in the human genome, or a total of six gen! es when β4GalT-I is included. The family elements are designated as β4GalT-I, -II, -III, -IV, -V and -VI, where β4GalT-I represents the previously well-characterized β4GalT recognized to function in lactose biosynthesis (15). The following diagram implys the chromosome number and stead of each of the gene family members. physical body 4: Schematic representation of the human 4GalT family members. The transcript representing the gene located on human chromosome 9p13 (4GalT-I) is shown at the top. The five additional family members (4GalT-II through -VI) are shown with their chromosomal location and mRNA size (from Northern blot analysis) noted. The open recess indicates coding sequence; the first three numbers indicate the number of amino acids in the stem region, catalytic landing field and unmown coding region, respectively. The total number of nucleotides in the coding region is also shown. Since the full-length 5?-untranslated region of each homolog ha s not been determined, this region is depicted by a belt along bill with the number of nucleotides obtained from the most 5?-clone indicated. The thin gentle wind at the right indicates the 3?-untranslated region with the number of nucleotides, available from the EST clones shown. As three of the homologs (4GalT-II,-V, and -VI) do not contain a consensus polyadenylation signal sequence (An), the predicted length of the 3?-untranslated region is give in italics. The sequence of 4GalT-II and -VI that was obtained by RACE, is 5?of the solid arrowhead. identify over on each mRNA is the rig of the transmembrane sphere (solid box) and the position of each Cys residue. The position, in 4GalT-I of the only intramolecular disulfide bond, Cys130 and Cys243 is indicated. Cys338 in the 4GalT-I sequence is replaced by a Tyr in each family member. acknowledgement of large family of ß (1,4) galactosyltransferaseSeveral groups independently used the emerging EST database information in 1 997 to identify a group of human cDNA sequences with ! similarities to the Graeco-Roman ß4Gal-T (designated ß4Gal-T1) (18, 19). Within 1 year, five novel human ß4Gal- T genes designated ß4Gal-T2 to -T6 were determine cloned, and enzymatic functions of their recombinant proteins demonstrated (18, 19).The two genes, ß4Gal-T5 and -T6, were determine by traditional re-create strategies as well as computer cloning (18). Recently, a seventh homologous gene designated ß4Gal-T7 was identified by the computer cloning strategy (18, 20). Its homology has not been conventional yet. BibliographyReferences1.Serum galactosyltransferase isoform changes in derelict arthritis, Alavi et al., J Rheumatol. 2004 Aug; 31(8):1513-20. 2. parvenu Insights into rheumatoid arthritis associated glycosylation changes, Alavi et al., Adv Exp Med Biol. 2005; 564:129-38. 3.Functional interaction between the SSeCKS support protein and the cytoplasmic domain of ß1,4-galactosyltransferase, Wassler et al., Journal of jail cell Science 114, 2291-2300 (2001)4.T umor gangrene Factor-α Microsatellite Polymorphism Association with Rheumatoid Arthritis in Indian patients, Agrawal, et al, pull in of Medical Research 36 (2005) 555?559. 5.

Changes in Normal Glycosylation Mechanisms in Autoimmune screaky Disease, Axford, et al., Glycosylation Mechanisms and Auloimmune Rheumatic Disease. 6.Structural analysis of the N-glycans from human immune globulin Al: comparison of normal human serum immune serum globulin Al with that separate from patients with rheumatoid arthritis, Field, et al, Biochem. J. (1994) 299, 261-275. 7.B lymphocyte galactosyltransferase protein in normal individuals and in patients with rheumatoid arthriti! s, Keusch, et al, Glycoconjugate Journal 15, 1093?1097 (1998)8.dbSNP: The NCBI database of genetic variation, Sherry, et al, Glycoconjugate Journal 15, 1093?1097 (1998)9.A be of human genome sequence variation containing 1.42 million single nucleotide polymorphisms, The International SNP comprise Working Group, (2001) disposition, 409: 928-93310.High-Throughput Identification, Database storage and Analysis of SNPs in EST Sequences, Useche et al. (2001), Genome Informatics 12: 194?20311.A general approach to single-nucleotide polymorphism discovery, Marth et al. (1999), genius transmitteds, 452-45612.dbSNP-Database for Single Nucleotide Polymorphisms and other Classes of Minor Genetic Variation. Sherry, S.T., Ward, M. and Sirotkin, K. (1999), Genome Research, 9, 677-67913.Reading Bits of Genetic Information: Methods for Single-Nucleotide Polymorphism Analysis, Landegren et al. (1998), Genome Research, 8:769-77614.Variations on a mind: cataloging human DNA sequence variation. Co llins, F.S., Guyer, M.S. & Chakravarti, A., (1997), Science 278, 1580?158115.The expanding b4-galactosyltransferase gene family: messages from the databanks. Neng-Wen Lo, Joel H.Shaper, Jonathan Pevsner and Nancy L.Shaper, (1998), MD 21287?8937, USA. 16.Glycosylation pathway in the biosynthesis of nonreducing terminal sequences oligosaccharides of glycoproteins, Beyer,T.A. and Hill,R.L., (1968), Horowitz,M. (ed.), The Glycoconjugates. Vol. III, Academic Press, New York, pp. 25?45. 17.The chicken genome contains two functional nonallelic b1,4-galactosyltransferase genes: chromosomal designation to syntenic regions tracks fate of the two gene lineages in the human genome, Shaper,N.L., Meurer,J.A., Joziasse,J.H., Chou,T.-D.D., Smith,E.J., Schnaar,R.L and Shaper,J.H., (1997), J.Biol. Chem., 272, 31389?31399. 18.Identifcation and painting of large galactosyltransferase genefamilies: galactosyltransferases for all functions, Margarida Amado, Raquel Almeida, Tilo Schwientek, Henrik Cl ausen, (1999), Biochimica et Biophysica Acta 1473 (19! 99) 35-53. 19.A Family of human ß4-galactosyltransferases: cloning and expression of two novel UDP-galactose: ß-n-acetylglucosamine ß1,4-galactosyltransferases, ß4Gal-T2and ß4Gal-T3, R Almeida, M. Amado, L. David, S.B. Levery, E.H. Holmes, G. Merkx, A.G. van Kessel, H. Hassan, E.P. Bennett, H. Clausen, J. Biol. Chem. 272 (1997) 31979-31992. 20.Cloning and expression of a proteoglycan UDP-galactose:ß-xylose ß1,4-galactosyltransferaseI. A seventh member of the human ß4-galactosyltransferase gene family, R. Almeida, S.B. Levery, U. Mandel, H. Kresse, T. Schwientek, E.P. Bennett, H. Clausen, J. Biol. Chem. 274 (1999) 26165-26171. 21.Use of site-directed mutagenesis to identify the galactosyltransferase binding sites for UDP-galactose, H. Zu, M.N. Fukuda, S.S. Wong, Y. Wang, Z. Liu, Q.Tang, H.E. Appert, Biochem. Biophys. Res. Commun. 206 (1995) 362-369.Mizuochi T., Taniguchi T, Shimizu A. and Kobata A. (1982), J. Immunol. 129, 2016-2020. 22.Malhotra R, Wormald M.R., Rudd P., Fisc her P.B., Dwek R.A. and Sim R.B. (1995), Nature Med. 1.237-243. 23.Roitt IM, Dwek R.A., Parekh R.B., Rademacher T.W., Alavi A, Axford J.S., Bodman K., Bond A., Cooke A., Hay F.C., et.al (1988). Recenti Progressi medicina 79. 314-317. 24.Abnormalities in immunoglobulin G glycosylation and immunologic disorders, Alavi A., Axford J.S., (1996) pp. 149-169, John Wiley and sons ltd, London. 25.Podolsky D.K., Weiser M.W., Westwood J.C. and Gammon M., (1997), J. Biol. Chem. 252. 1807-1813. 26.Serum galactosyl transferase as a marker of disease activity in rheumatoid arthritis, Azita Alavi, Axford J.S., (1997), Biochemical rescript proceeding 25., 313. 27.Role of PTPN22 in type 1 diabetes and other autoimmune diseases, Bottini N, Vang T, Cucca F, Mustelin T., (2006 may 10), Semin Immunol. If you want to get a full essay, order it on our website: BestEssayCheap.com

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